Novel Citronellyl-Based Photoprobes Designed to Identify ER Proteins Interacting with Dolichyl Phosphate in Yeast and Mammalian Cells.

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Novel Citronellyl-Based Photoprobes Designed to Identify ER Proteins Interacting with Dolichyl Phosphate in Yeast and Mammalian Cells.

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

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2015年論文

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2015年論文

@zh-tw

2015年论文

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2015年论文

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2015年论文

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name

Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

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Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

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type

Item

label

Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

@ast

Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

@en

prefLabel

Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

@ast

Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

@en

P1476

Novel Citronellyl-Based Photop ...... in Yeast and Mammalian Cells.

@en

P2093

Charles J Waechter

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Fredrick O Onono

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H Peter Spielmann

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Jeffrey S Rush

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Karunai Leela Subramanian

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Thangaiah Subramanian

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P2860

Human dolichol-phosphate-mannose synthase consists of three subunits, DPM1, DPM2 and DPM3

Nogo-B receptor is necessary for cellular dolichol biosynthesis and protein N-glycosylation

DPM2 regulates biosynthesis of dolichol phosphate-mannose in mammalian cells: correct subcellular localization and stabilization of DPM1, and binding of dolichol phosphate

Nogo-B receptor stabilizes Niemann-Pick type C2 protein and regulates intracellular cholesterol trafficking

An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli

An O-antigen processing function for Wzx (RfbX): a promising candidate for O-unit flippase

Role of Flippases in Protein Glycosylation in the Endoplasmic Reticulum

Structure and mechanism of an active lipid-linked oligosaccharide flippase

The CWH8 gene encodes a dolichyl pyrophosphate phosphatase with a luminally oriented active site in the endoplasmic reticulum of Saccharomyces cerevisiae.

Alg14 recruits Alg13 to the cytoplasmic face of the endoplasmic reticulum to form a novel bipartite UDP-N-acetylglucosamine transferase required for the second step of N-linked glycosylation.

P304

123-141

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P31

scholarly article

P356

10.2174/2212796810666160216221610

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2015-01-01T00:00:00Z

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P698

27099830

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P921

protein design

P932

4834925

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